Complex structure of SidM/DrrA with the wild type Rab1. Determined by X-ray diffraction at 2.85 Å resolution. Released 22 Dec 2009.
Explore 3L0I in 3D Show helices and sheets RCSB PDB PDBe
3L0I contains 48 α-helices and 22 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 214-224 | 11 | |
| α-helix | 229-231 | 3 | |
| β-strand | 239 | 1 | 1 |
| α-helix | 240 | 1 | |
| α-helix | 241-245 | 5 | |
| α-helix | 246-258 | 13 | |
| α-helix | 271-280 | 10 | |
| α-helix | 286-307 | 22 | |
| β-strand | 316 | 1 | 1 |
| α-helix | 320-322 | 3 | |
| α-helix | 323-361 | 39 | |
| α-helix | 365-381 | 17 | |
| α-helix | 386-389 | 4 | |
| α-helix | 391-393 | 3 | |
| α-helix | 400-419 | 20 | |
| α-helix | 428-447 | 20 | |
| α-helix | 449 | 1 | |
| α-helix | 464-478 | 15 | |
| β-strand | 484-485 | 2 | 2 |
| β-strand | 488-489 | 2 | 2 |
| α-helix | 490-506 | 17 | |
| α-helix | 512-519 | 8 | |
| α-helix | 526-529 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 3 |
| β-strand | 32 | 1 | 3 |
| α-helix | 39-44 | 6 | |
| β-strand | 48-55 | 8 | 3 |
| β-strand | 58-65 | 8 | 3 |
| β-strand | 86-89 | 4 | 3 |
| α-helix | 97-110 | 14 | |
| β-strand | 118-121 | 4 | 3 |
| α-helix | 141-144 | 4 | |
| β-strand | 150 | 1 | 3 |
| α-helix | 159-168 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 211-222 | 12 | |
| α-helix | 223-227 | 5 | |
| α-helix | 230-232 | 3 | |
| β-strand | 237-239 | 3 | 4 |
| α-helix | 241-245 | 5 | |
| α-helix | 246-259 | 14 | |
| α-helix | 271-280 | 10 | |
| α-helix | 286-309 | 24 | |
| β-strand | 316-318 | 3 | 4 |
| α-helix | 319-361 | 43 | |
| α-helix | 365-381 | 17 | |
| α-helix | 386-389 | 4 | |
| α-helix | 390-393 | 4 | |
| α-helix | 400-419 | 20 | |
| α-helix | 428-447 | 20 | |
| α-helix | 452-454 | 3 | |
| α-helix | 464-478 | 15 | |
| β-strand | 484-485 | 2 | 5 |
| β-strand | 488-489 | 2 | 5 |
| α-helix | 490-506 | 17 | |
| α-helix | 512-519 | 8 | |
| α-helix | 526-529 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-18 | 9 | 6 |
| α-helix | 24-28 | 5 | |
| β-strand | 32 | 1 | 6 |
| α-helix | 39-44 | 6 | |
| β-strand | 48-55 | 8 | 6 |
| β-strand | 58-65 | 8 | 6 |
| α-helix | 70-72 | 3 | |
| α-helix | 78-81 | 4 | |
| β-strand | 86-92 | 7 | 6 |
| α-helix | 96-112 | 17 | |
| β-strand | 118-124 | 7 | 6 |
| α-helix | 136-145 | 10 | |
| β-strand | 150-153 | 4 | 6 |
| α-helix | 159-174 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DrrA | A, C | protein | 363 | Legionella pneumophila | Q5ZSQ3 (AlphaFold model) |
| Ras-related protein Rab-1A | B, D | protein | 199 | Homo sapiens | P62820 (AlphaFold model) |
>3L0I_1 DrrA (chains A, C) GPLGSPRYELGEELRDKIKQEPSFSNMVSAKKFYNKAIKDFTAPKEGAEVVSVKTHIMRP IDFMLMGLREEFNLYSEDGAHLSAPGTIRLLREKNLLPEEQIARIESVYNQAMSKRFELH AEHKKEHDEMPYSDAKAMLDEVAKIRELGVQRVTRIENLENAKKLWDNANSMLEKGNISG YLKAANELHKFMKEKNLKEDDLRPELSDKTISPKGYAILQSLWGAASDYSRAAATLTEST VEPGLVSAVNKMSAFFMDCKLSPNERATPDPDFKVGKSKILVGIMQFIKDVADPTSKIWM HNTKALMNHKIAAIQKLERSNNVNDETLESVLSSKGENLSEYLSYKYATKDEGREHRYTA STE
>3L0I_2 Ras-related protein Rab-1A (chains B, D) MGSSHHHHHHSSGENLYFQGRPMSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTE SYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQES FNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNA TNVEQSFMTMAAEIKKRMG
Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Zhu, Y., Hu, L., Zhou, Y. et al. Proc Natl Acad Sci U S A (2010) 107:4699-4704. DOI 10.1073/pnas.0914231107 · PubMed
Other PDB entries of the same protein (UniProt Q5ZSQ3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3L0I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.